ID BAG4_HUMAN Reviewed; 457 AA. AC O95429; B4E217; O95818; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 193. DE RecName: Full=BAG family molecular chaperone regulator 4; DE Short=BAG-4; DE AltName: Full=Bcl-2-associated athanogene 4; DE AltName: Full=Silencer of death domains; GN Name=BAG4; Synonyms=SODD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Leukemic T-cell; RX PubMed=9873016; DOI=10.1074/jbc.274.2.781; RA Takayama S., Xie Z., Reed J.C.; RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone RT regulators."; RL J. Biol. Chem. 274:781-786(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TNFRSF1A AND RP TNFRSF12. RC TISSUE=Leukemic T-cell; RX PubMed=9915703; DOI=10.1126/science.283.5401.543; RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.; RT "Prevention of constitutive TNF receptor 1 signaling by silencer of death RT domains."; RL Science 283:543-546(1999). RN [3] RP ERRATUM OF PUBMED:9915703. RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.; RL Science 283:1852-1852(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [8] RP FUNCTION, AND INTERACTION WITH PRKN. RX PubMed=24270810; DOI=10.1038/nature12748; RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., RA Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.; RT "High-content genome-wide RNAi screens identify regulators of parkin RT upstream of mitophagy."; RL Nature 504:291-295(2013). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-53; ARG-108 AND ARG-185, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [11] RP STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, AND MUTAGENESIS OF RP GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446. RX PubMed=12058034; DOI=10.1074/jbc.m202792200; RA Briknarova K., Takayama S., Homma S., Baker K., Cabezas E., Hoyt D.W., RA Li Z., Satterthwait A.C., Ely K.R.; RT "BAG4/SODD protein contains a short BAG domain."; RL J. Biol. Chem. 277:31172-31178(2002). CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting CC substrate release (By similarity). Prevents constitutive TNFRSF1A CC signaling. Negative regulator of PRKN translocation to damaged CC mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}. CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to CC the death domain of TNFRSF1A in the absence of TNF and thereby prevents CC binding of adapter molecules such as TRADD or TRAF2. Binds to the death CC domain of TNFRSF12. Interacts with PRKN. {ECO:0000269|PubMed:12058034, CC ECO:0000269|PubMed:24270810, ECO:0000269|PubMed:9915703}. CC -!- INTERACTION: CC O95429; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-2949658, EBI-11096309; CC O95429; O00154-4: ACOT7; NbExp=3; IntAct=EBI-2949658, EBI-12007918; CC O95429; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2949658, EBI-10173507; CC O95429; Q9NP73-4: ALG13; NbExp=3; IntAct=EBI-2949658, EBI-10186621; CC O95429; Q03989: ARID5A; NbExp=3; IntAct=EBI-2949658, EBI-948603; CC O95429; Q7L5A3: ATOSB; NbExp=5; IntAct=EBI-2949658, EBI-745689; CC O95429; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-2949658, EBI-12811889; CC O95429; A8KA13: BCL6B; NbExp=3; IntAct=EBI-2949658, EBI-10174813; CC O95429; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-2949658, EBI-2548012; CC O95429; Q5JPI3-2: C3orf38; NbExp=4; IntAct=EBI-2949658, EBI-12009184; CC O95429; P42575: CASP2; NbExp=3; IntAct=EBI-2949658, EBI-520342; CC O95429; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-2949658, EBI-11954144; CC O95429; Q8IXM7: CIMAP1C; NbExp=3; IntAct=EBI-2949658, EBI-13331299; CC O95429; Q9NPI6: DCP1A; NbExp=5; IntAct=EBI-2949658, EBI-374238; CC O95429; Q8IZD4: DCP1B; NbExp=2; IntAct=EBI-2949658, EBI-521595; CC O95429; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2949658, EBI-742054; CC O95429; Q99615: DNAJC7; NbExp=2; IntAct=EBI-2949658, EBI-357552; CC O95429; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-2949658, EBI-948630; CC O95429; Q12805: EFEMP1; NbExp=3; IntAct=EBI-2949658, EBI-536772; CC O95429; Q96A10: ERVK3-1; NbExp=3; IntAct=EBI-2949658, EBI-10486892; CC O95429; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-2949658, EBI-2807642; CC O95429; O95363: FARS2; NbExp=3; IntAct=EBI-2949658, EBI-2513774; CC O95429; P02794: FTH1; NbExp=4; IntAct=EBI-2949658, EBI-713259; CC O95429; P06241-3: FYN; NbExp=3; IntAct=EBI-2949658, EBI-10691738; CC O95429; O95872: GPANK1; NbExp=3; IntAct=EBI-2949658, EBI-751540; CC O95429; Q13227: GPS2; NbExp=3; IntAct=EBI-2949658, EBI-713355; CC O95429; P49639: HOXA1; NbExp=3; IntAct=EBI-2949658, EBI-740785; CC O95429; P34931: HSPA1L; NbExp=4; IntAct=EBI-2949658, EBI-354912; CC O95429; P54652: HSPA2; NbExp=5; IntAct=EBI-2949658, EBI-356991; CC O95429; P17066: HSPA6; NbExp=3; IntAct=EBI-2949658, EBI-355106; CC O95429; P11142: HSPA8; NbExp=6; IntAct=EBI-2949658, EBI-351896; CC O95429; P53990-3: IST1; NbExp=3; IntAct=EBI-2949658, EBI-12188567; CC O95429; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-2949658, EBI-2511344; CC O95429; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-2949658, EBI-11954971; CC O95429; P33176: KIF5B; NbExp=3; IntAct=EBI-2949658, EBI-355878; CC O95429; Q3LI77: KRTAP13-4; NbExp=3; IntAct=EBI-2949658, EBI-11953996; CC O95429; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-2949658, EBI-739863; CC O95429; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-2949658, EBI-10172511; CC O95429; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-2949658, EBI-11958132; CC O95429; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-2949658, EBI-11993254; CC O95429; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2949658, EBI-9088686; CC O95429; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-2949658, EBI-716006; CC O95429; A8MW99: MEI4; NbExp=3; IntAct=EBI-2949658, EBI-19944212; CC O95429; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-2949658, EBI-744402; CC O95429; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-2949658, EBI-5662487; CC O95429; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-2949658, EBI-2858213; CC O95429; Q14990: ODF1; NbExp=3; IntAct=EBI-2949658, EBI-10234557; CC O95429; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-2949658, EBI-10181968; CC O95429; O75340: PDCD6; NbExp=3; IntAct=EBI-2949658, EBI-352915; CC O95429; Q9UBV8: PEF1; NbExp=5; IntAct=EBI-2949658, EBI-724639; CC O95429; O15173: PGRMC2; NbExp=5; IntAct=EBI-2949658, EBI-1050125; CC O95429; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-2949658, EBI-2339674; CC O95429; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-2949658, EBI-12226639; CC O95429; P28074: PSMB5; NbExp=5; IntAct=EBI-2949658, EBI-357828; CC O95429; Q53H96: PYCR3; NbExp=3; IntAct=EBI-2949658, EBI-2959680; CC O95429; Q9BTL3: RAMAC; NbExp=6; IntAct=EBI-2949658, EBI-744023; CC O95429; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-2949658, EBI-12001422; CC O95429; Q9UPU9-3: SAMD4A; NbExp=3; IntAct=EBI-2949658, EBI-11986417; CC O95429; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-2949658, EBI-3957636; CC O95429; Q7Z5V6-2: SAXO4; NbExp=6; IntAct=EBI-2949658, EBI-12000762; CC O95429; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-2949658, EBI-2130111; CC O95429; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-2949658, EBI-11522811; CC O95429; P14678-2: SNRPB; NbExp=5; IntAct=EBI-2949658, EBI-372475; CC O95429; P09234: SNRPC; NbExp=3; IntAct=EBI-2949658, EBI-766589; CC O95429; O75177-5: SS18L1; NbExp=3; IntAct=EBI-2949658, EBI-12035119; CC O95429; P51687: SUOX; NbExp=3; IntAct=EBI-2949658, EBI-3921347; CC O95429; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-2949658, EBI-13092532; CC O95429; Q9P0N9: TBC1D7; NbExp=5; IntAct=EBI-2949658, EBI-3258000; CC O95429; O95988: TCL1B; NbExp=3; IntAct=EBI-2949658, EBI-727338; CC O95429; Q96M29: TEKT5; NbExp=3; IntAct=EBI-2949658, EBI-10239812; CC O95429; Q7Z6R9: TFAP2D; NbExp=5; IntAct=EBI-2949658, EBI-11952651; CC O95429; Q9GZM7: TINAGL1; NbExp=3; IntAct=EBI-2949658, EBI-715869; CC O95429; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2949658, EBI-11741437; CC O95429; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-2949658, EBI-8451480; CC O95429; Q99816: TSG101; NbExp=3; IntAct=EBI-2949658, EBI-346882; CC O95429; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2949658, EBI-10180829; CC O95429; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-2949658, EBI-12817837; CC O95429; Q9UPT9-2: USP22; NbExp=3; IntAct=EBI-2949658, EBI-12074414; CC O95429; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-2949658, EBI-2559305; CC O95429; Q96K62: ZBTB45; NbExp=3; IntAct=EBI-2949658, EBI-714373; CC O95429; O15062: ZBTB5; NbExp=3; IntAct=EBI-2949658, EBI-722671; CC O95429; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-2949658, EBI-11962760; CC O95429; Q53FC7; NbExp=2; IntAct=EBI-2949658, EBI-9356749; CC O95429; Q96EJ4; NbExp=3; IntAct=EBI-2949658, EBI-750454; CC O95429; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-2949658, EBI-25475850; CC O95429; PRO_0000449622 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2949658, EBI-25475862; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95429-1; Sequence=Displayed; CC Name=2; CC IsoId=O95429-2; Sequence=VSP_042741; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF095194; AAD16123.2; -; mRNA. DR EMBL; AF111116; AAD05226.1; -; mRNA. DR EMBL; AK304072; BAG64979.1; -; mRNA. DR EMBL; AC084024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038505; AAH38505.2; -; mRNA. DR CCDS; CCDS56533.1; -. [O95429-2] DR CCDS; CCDS6104.1; -. [O95429-1] DR RefSeq; NP_001191807.1; NM_001204878.1. [O95429-2] DR RefSeq; NP_004865.1; NM_004874.3. [O95429-1] DR PDB; 1M62; NMR; -; A=376-457. DR PDB; 1M7K; NMR; -; A=358-456. DR PDBsum; 1M62; -. DR PDBsum; 1M7K; -. DR AlphaFoldDB; O95429; -. DR SMR; O95429; -. DR BioGRID; 114906; 240. DR IntAct; O95429; 170. DR MINT; O95429; -. DR STRING; 9606.ENSP00000287322; -. DR GlyGen; O95429; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O95429; -. DR PhosphoSitePlus; O95429; -. DR BioMuta; BAG4; -. DR EPD; O95429; -. DR jPOST; O95429; -. DR MassIVE; O95429; -. DR MaxQB; O95429; -. DR PaxDb; 9606-ENSP00000287322; -. DR PeptideAtlas; O95429; -. DR ProteomicsDB; 50875; -. [O95429-1] DR ProteomicsDB; 50876; -. [O95429-2] DR Pumba; O95429; -. DR Antibodypedia; 4434; 449 antibodies from 43 providers. DR DNASU; 9530; -. DR Ensembl; ENST00000287322.5; ENSP00000287322.4; ENSG00000156735.11. [O95429-1] DR Ensembl; ENST00000432471.6; ENSP00000393298.2; ENSG00000156735.11. [O95429-2] DR GeneID; 9530; -. DR KEGG; hsa:9530; -. DR MANE-Select; ENST00000287322.5; ENSP00000287322.4; NM_004874.4; NP_004865.1. DR UCSC; uc003xky.3; human. [O95429-1] DR AGR; HGNC:940; -. DR CTD; 9530; -. DR DisGeNET; 9530; -. DR GeneCards; BAG4; -. DR HGNC; HGNC:940; BAG4. DR HPA; ENSG00000156735; Low tissue specificity. DR MIM; 603884; gene. DR neXtProt; NX_O95429; -. DR OpenTargets; ENSG00000156735; -. DR PharmGKB; PA25240; -. DR VEuPathDB; HostDB:ENSG00000156735; -. DR eggNOG; KOG4361; Eukaryota. DR GeneTree; ENSGT00940000158936; -. DR HOGENOM; CLU_051025_0_0_1; -. DR InParanoid; O95429; -. DR OMA; WNSARPR; -. DR OrthoDB; 5320815at2759; -. DR PhylomeDB; O95429; -. DR TreeFam; TF102013; -. DR PathwayCommons; O95429; -. DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response. DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease. DR Reactome; R-HSA-75893; TNF signaling. DR Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions. DR SignaLink; O95429; -. DR SIGNOR; O95429; -. DR BioGRID-ORCS; 9530; 26 hits in 1159 CRISPR screens. DR ChiTaRS; BAG4; human. DR EvolutionaryTrace; O95429; -. DR GeneWiki; BAG4; -. DR GenomeRNAi; 9530; -. DR Pharos; O95429; Tbio. DR PRO; PR:O95429; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; O95429; Protein. DR Bgee; ENSG00000156735; Expressed in Brodmann (1909) area 23 and 188 other cell types or tissues. DR ExpressionAtlas; O95429; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0051087; F:protein-folding chaperone binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc. DR GO; GO:0090367; P:negative regulation of mRNA modification; IEA:Ensembl. DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl. DR GO; GO:0006457; P:protein folding; TAS:ProtInc. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central. DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl. DR Gene3D; 1.20.58.120; BAG domain; 1. DR InterPro; IPR039773; BAG_chaperone_regulator. DR InterPro; IPR036533; BAG_dom_sf. DR InterPro; IPR003103; BAG_domain. DR PANTHER; PTHR12329:SF10; BAG FAMILY MOLECULAR CHAPERONE REGULATOR 4; 1. DR PANTHER; PTHR12329; BCL2-ASSOCIATED ATHANOGENE; 1. DR Pfam; PF02179; BAG; 1. DR SMART; SM00264; BAG; 1. DR SUPFAM; SSF63491; BAG domain; 1. DR PROSITE; PS51035; BAG; 1. DR Genevisible; O95429; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chaperone; Cytoplasm; Methylation; KW Phosphoprotein; Reference proteome. FT CHAIN 1..457 FT /note="BAG family molecular chaperone regulator 4" FT /id="PRO_0000088870" FT DOMAIN 379..456 FT /note="BAG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369" FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 113..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 347..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..50 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..136 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 166..191 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 265..280 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 281..295 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 296..333 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..370 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 40 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 53 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 108 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 185 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 90..125 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042741" FT MUTAGEN 414 FT /note="E->A: Reduces interaction with HSP70." FT /evidence="ECO:0000269|PubMed:12058034" FT MUTAGEN 424 FT /note="D->A: Abolishes interaction with HSP70." FT /evidence="ECO:0000269|PubMed:12058034" FT MUTAGEN 438..439 FT /note="RK->AA: Reduces interaction with HSP70." FT /evidence="ECO:0000269|PubMed:12058034" FT MUTAGEN 446 FT /note="Q->A: Abolishes interaction with HSP70." FT /evidence="ECO:0000269|PubMed:12058034" FT HELIX 380..399 FT /evidence="ECO:0007829|PDB:1M62" FT HELIX 407..423 FT /evidence="ECO:0007829|PDB:1M62" FT HELIX 432..456 FT /evidence="ECO:0007829|PDB:1M62" SQ SEQUENCE 457 AA; 49594 MW; B89D59E8118684A3 CRC64; MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL //